Molecular & Cellular Biology Program firstname.lastname@example.org University of Iowa 357 Medical Research Center Iowa City, IA 52242-1182 Phone: 319-335-7748 Fax: 319-335-7656
Elucidating the mechanisms by which the UPR tailors specific responses to ER stress.
Adaptation and stress response pathways have evolved to allow cells to adapt to their environment. Cells are able to interpret stress and respond by activating certain gene profiles that will help deal with the insult and return to a homeostatic state. In the case of the endoplasmic reticulum (ER) stress comes in the form of misfolded or unfolded proteins. The unfolded protein response (UPR) is a transcriptional program which helps alleviate stress through increased folding or efficiency of ER function. However, the UPR can also lead to apoptosis if it is unable to clear the stress. We hope to elucidate how the different components of the UPR sense the nature, strength and persistence of a stimulus and how these interactions decide cell fate and response. We will evaluate the contribution of individual parts of the UPR and how their interrelationship can lead to differing outputs. The use of knockout models of key components, as well as computational modeling, will allow us to understand the complexities behind the UPR.
Mao HZ, Ehrhardt N, Bedoya C, Gomez JA, DeZwaan-McCabe D, Mungrue IN, Kaufman RJ, Rutkowski DT, Péterfy M. Lipase maturation factor 1 (lmf1) is induced by endoplasmic reticulum stress through activating transcription factor 6α (Atf6α) signaling. J Biol Chem. 2014 Aug 29;289(35):24417-27. doi:10.1074/jbc.M114.588764. Epub 2014 Jul 17. PubMed PMID: 25035425; PubMed Central PMCID: PMC4148868.
Gomez JA, Tyra HM, DeZwaan-McCabe D, Olievier AK, and Rutkowski DT. Synthetic embroynic lethality upon deletion of the ER cochaperone p58IPK and the ER stess sensor ATF6alpha. Biochem Biophys Res Comm 443:115-119, 2014.
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